Proteopedia:Featured EDU/1: Difference between revisions
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<tr><td>[[Image:Phi-psi-clashes-1.png|center|300px]]</td></tr> | <tr><td>[[Image:Phi-psi-clashes-1.png|center|300px]]</td></tr> | ||
<tr><td>'''Tutorial: The Ramachandran principle, phi (φ) and psi (ψ) angles in proteins'''</td></tr> | <tr><td>'''Tutorial: The Ramachandran principle, phi (φ) and psi (ψ) angles in proteins'''</td></tr> | ||
<tr><td>''Eric Martz''</td></tr> | <tr><td>''by Eric Martz''</td></tr> | ||
<tr><td> | <tr><td> | ||
<div class="scrolling"> | <div class="scrolling"> | ||
The Ramachandran Principle says that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt, because most other conformations are impossible due to steric collisions between atoms. | The Ramachandran Principle says that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt, because most other conformations are impossible due to steric collisions between atoms. | ||
Check Show Clashes to see where non-bonded atoms are overlapping, and thus in physically impossible positions. | Check Show Clashes to see where non-bonded atoms are overlapping, and thus in physically impossible positions. | ||
</div> | </div> | ||
</td></tr> | </td></tr> | ||
</table> | </table> |